Ginsentides: Cysteine and Glycine-rich Peptides from the Ginseng Family with Unusual Disulfide Connectivity. Issue 1 (December 2018)
- Record Type:
- Journal Article
- Title:
- Ginsentides: Cysteine and Glycine-rich Peptides from the Ginseng Family with Unusual Disulfide Connectivity. Issue 1 (December 2018)
- Main Title:
- Ginsentides: Cysteine and Glycine-rich Peptides from the Ginseng Family with Unusual Disulfide Connectivity
- Authors:
- Tam, James P.
Nguyen, Giang
Loo, Shining
Wang, Shujing
Yang, Daiwen
Kam, Antony - Abstract:
- Abstract Ginseng, a popular and valuable traditional medicine, has been used for centuries to maintain health and treat disease. Here we report the discovery and characterization of ginsentides, a novel family of cysteine and glycine-rich peptides derived from the three most widely-used ginseng species:Panax ginseng, Panax quinquefolius, andPanax notoginseng . Using proteomic and transcriptomic methods, we identified 14 ginsentides, TP1-TP14 which consist of 31–33 amino acids and whose expression profiles are species- and tissues-dependent. Ginsentides have an eight-cysteine motif typical of the eight-cysteine-hevein-like peptides (8C-HLP) commonly found in medicinal herbs, but lack a chitin-binding domain. Transcriptomic analysis showed that the three-domain biosynthetic precursors of ginsentides differ from known 8C-HLP precursors in architecture and the absence of a C-terminal protein-cargo domain. A database search revealed an additional 50 ginsentide-like precursors from both gymnosperms and angiosperms. Disulfide mapping and structure determination of the ginsentide TP1 revealed a novel disulfide connectivity that differs from the 8C-HLPs. The structure of ginsentide TP1 is highly compact, with the N- and C-termini topologically fixed by disulfide bonds to form a pseudocyclic structure that confers resistance to heat, proteolysis, and acid and serum-mediated degradation. Together, our results expand the chemical space of natural products found in ginseng and highlightAbstract Ginseng, a popular and valuable traditional medicine, has been used for centuries to maintain health and treat disease. Here we report the discovery and characterization of ginsentides, a novel family of cysteine and glycine-rich peptides derived from the three most widely-used ginseng species:Panax ginseng, Panax quinquefolius, andPanax notoginseng . Using proteomic and transcriptomic methods, we identified 14 ginsentides, TP1-TP14 which consist of 31–33 amino acids and whose expression profiles are species- and tissues-dependent. Ginsentides have an eight-cysteine motif typical of the eight-cysteine-hevein-like peptides (8C-HLP) commonly found in medicinal herbs, but lack a chitin-binding domain. Transcriptomic analysis showed that the three-domain biosynthetic precursors of ginsentides differ from known 8C-HLP precursors in architecture and the absence of a C-terminal protein-cargo domain. A database search revealed an additional 50 ginsentide-like precursors from both gymnosperms and angiosperms. Disulfide mapping and structure determination of the ginsentide TP1 revealed a novel disulfide connectivity that differs from the 8C-HLPs. The structure of ginsentide TP1 is highly compact, with the N- and C-termini topologically fixed by disulfide bonds to form a pseudocyclic structure that confers resistance to heat, proteolysis, and acid and serum-mediated degradation. Together, our results expand the chemical space of natural products found in ginseng and highlight the occurrence, distribution, disulfide connectivity, and precursor architectures of cysteine- and glycine-rich ginsentides as a class of novel non-chitin-binding, non-cargo-carrying 8C-HLPs. … (more)
- Is Part Of:
- Scientific reports. Volume 8:Issue 1(2018)
- Journal:
- Scientific reports
- Issue:
- Volume 8:Issue 1(2018)
- Issue Display:
- Volume 8, Issue 1 (2018)
- Year:
- 2018
- Volume:
- 8
- Issue:
- 1
- Issue Sort Value:
- 2018-0008-0001-0000
- Page Start:
- 1
- Page End:
- 15
- Publication Date:
- 2018-12
- Subjects:
- Natural history -- Research -- Periodicals
Biology -- Research -- Periodicals
Physical sciences -- Research -- Periodicals
Earth sciences -- Research -- Periodicals
Environmental sciences -- Research -- Periodicals
502.85 - Journal URLs:
- http://www.nature.com/ ↗
http://www.nature.com/srep/index.html ↗ - DOI:
- 10.1038/s41598-018-33894-x ↗
- Languages:
- English
- ISSNs:
- 2045-2322
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 10988.xml